Induction and Functional Analysis of Two Reduced Nicotinamide Adenine Dinucleotide Phosphate-dependent Glutathione Peroxidase-like Proteins in Synechocystis PCC 6803 During the Progression of Oxidative Stress

Overview

Journal Plant Physiol

Specialty Physiology

Date 2004 Sep 7

PMID 15347790

Citations 11

Authors

Ahmed Gaber

Kazuya Yoshimura

Masahiro Tamoi

Toru Takeda

Yoshihisa Nakano

Shigeru Shigeoka

Affiliations

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Abstract

Synechocystis PCC 6803 contains two types of glutathione peroxidase-like proteins (GPX-1 and GPX-2) that utilize NADPH but not reduced glutathione and unsaturated fatty acid hydroperoxides or alkyl hydroperoxides. The steady-state transcript level of gpx-1 gradually increased under oxidative stress conditions imposed by high light intensity, high salinity, or application of methylviologen or t-butyl hydroperoxide in the wild-type and GPX-2 knock-out mutant (gpx-2Delta) cells. To examine the ability of GPX-1, GPX-2, and thioredoxin peroxidase to scavenge lipid hydroperoxide in vivo, we measured the photosynthetic evolution of O(2) and the level of lipid peroxidation in the wild-type and each type of mutant cell after the application of t-butyl hydroperoxide or H(2)O(2). The data reported here indicate that GPX-1 and GPX-2 are essential for the removal of lipid hydroperoxides under normal and stress conditions, leading to the protection of membrane integrity.

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